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Database: UniProt/TrEMBL
Entry: G0HLK1_THES4
LinkDB: G0HLK1_THES4
Original site: G0HLK1_THES4 
ID   G0HLK1_THES4            Unreviewed;       559 AA.
AC   G0HLK1;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   25-OCT-2017, entry version 40.
DE   RecName: Full=DNA ligase {ECO:0000256|HAMAP-Rule:MF_00407};
DE            EC=6.5.1.6 {ECO:0000256|HAMAP-Rule:MF_00407};
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP/NAD(+)] {ECO:0000256|HAMAP-Rule:MF_00407};
GN   Name=lig {ECO:0000256|HAMAP-Rule:MF_00407};
GN   OrderedLocusNames=GQS_07890 {ECO:0000313|EMBL:AEK73474.1};
OS   Thermococcus sp. (strain CGMCC 1.5172 / 4557).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=1042877 {ECO:0000313|EMBL:AEK73474.1, ECO:0000313|Proteomes:UP000000874};
RN   [1] {ECO:0000313|EMBL:AEK73474.1, ECO:0000313|Proteomes:UP000000874}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.5172 / 4557 {ECO:0000313|Proteomes:UP000000874};
RX   PubMed=21914870; DOI=10.1128/JB.05851-11;
RA   Wang X., Gao Z., Xu X., Ruan L.;
RT   "Complete genome sequence of Thermococcus sp. strain 4557, a
RT   hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent
RT   area.";
RL   J. Bacteriol. 193:5544-5545(2011).
CC   -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA
CC       during DNA replication, DNA recombination and DNA repair.
CC       {ECO:0000256|HAMAP-Rule:MF_00407}.
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + diphosphate. {ECO:0000256|HAMAP-Rule:MF_00407}.
CC   -!- CATALYTIC ACTIVITY: NAD(+) + (deoxyribonucleotide)(n)-3'-hydroxyl
CC       + 5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m)
CC       + AMP + beta-nicotinamide D-nucleotide. {ECO:0000256|HAMAP-
CC       Rule:MF_00407}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00407};
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00407, ECO:0000256|RuleBase:RU004196}.
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DR   EMBL; CP002920; AEK73474.1; -; Genomic_DNA.
DR   RefSeq; WP_014013156.1; NC_015865.1.
DR   ProteinModelPortal; G0HLK1; -.
DR   STRING; 1042877.GQS_07890; -.
DR   EnsemblBacteria; AEK73474; AEK73474; GQS_07890.
DR   GeneID; 11016253; -.
DR   KEGG; the:GQS_07890; -.
DR   PATRIC; fig|1042877.9.peg.1532; -.
DR   eggNOG; arCOG01347; Archaea.
DR   eggNOG; COG1793; LUCA.
DR   KO; K10747; -.
DR   OMA; ETVCNIG; -.
DR   OrthoDB; POG093Z03L0; -.
DR   Proteomes; UP000000874; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0051103; P:DNA ligation involved in DNA repair; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.3260.10; -; 1.
DR   HAMAP; MF_00407; DNA_ligase; 1.
DR   InterPro; IPR022865; DNA_ligae_ATP-dep_bac/arc.
DR   InterPro; IPR000977; DNA_ligase_ATP-dep.
DR   InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR   InterPro; IPR012308; DNA_ligase_ATP-dep_N.
DR   InterPro; IPR036599; DNA_ligase_N_sf.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF04675; DNA_ligase_A_N; 1.
DR   SUPFAM; SSF117018; SSF117018; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00574; dnl1; 1.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000874};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00407};
KW   DNA recombination {ECO:0000256|HAMAP-Rule:MF_00407};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00407};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00407, ECO:0000313|EMBL:AEK73474.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00407};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   DOMAIN      327    455       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   ACT_SITE    249    249       N6-AMP-lysine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     247    247       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     254    254       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     269    269       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     299    299       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     339    339       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     414    414       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     420    420       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   559 AA;  63338 MW;  D415CBE4FF3B6BA9 CRC64;
     MKYAELADLY RRLEKTTLKT LKTKFVSDFL KKAPDELLDI IPYLILGKVF PDWDERELGV
     GEKLLIKAVS MATGVPEREI ENSVRDTGDL GESVALALKK KKQKSFFSQP LTIKRVYDTF
     MKIAEASGQG SQDRKLKYLA NLFMDAQPEE GKYLARTVLG TMRTGVAEGL MRDAIASAFG
     VKAELVERAY MLTSDFGYVA RVAKLEGNEG LSKVRIQVGK PIRPMLAQNA ANVKEALVEM
     GGKAAFEVKY DGARVQVHKD GDRVVIYSRR LENVTRSIPE VVDAVLESVK PEKAIVEGEL
     VAVGEGGKPR PFQYVLRRFR RKYNIEEMVE KIPLELNLFD VLYVDGDGMI DTPFSERRKK
     LEEIISQNER IRLAEQLVTT SADEAEEFYQ RALELGHEGL MAKRLDSVYE PGNRGKKWLK
     IKPTMEDLDL VIIGAEWGEG RRAHLLGSFL VAAFDPHSGE FVPVGKVGSG FTDEDLAEFT
     RMLKPLIVRE EGKYVEIEPK VVIQVTYQEI QKSPKYESGF ALRFPRYVAL REDKSPEEAD
     TIERIAQLYE FQERFKAKR
//
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